RUVB_DEIRA
ID RUVB_DEIRA Reviewed; 333 AA.
AC Q9X719;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Holliday junction ATP-dependent DNA helicase RuvB {ECO:0000255|HAMAP-Rule:MF_00016};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_00016};
GN Name=ruvB {ECO:0000255|HAMAP-Rule:MF_00016}; OrderedLocusNames=DR_0596;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=9447236; DOI=10.1016/s0921-8777(97)00048-7;
RA Kitayama S., Kohoroku M., Takagi A., Itoh H.;
RT "Mutation of D. radiodurans in a gene homologous to ruvB of E. coli.";
RL Mutat. Res. 385:151-157(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
CC -!- FUNCTION: The RuvA-RuvB complex in the presence of ATP renatures
CC cruciform structure in supercoiled DNA with palindromic sequence,
CC indicating that it may promote strand exchange reactions in homologous
CC recombination. RuvAB is a helicase that mediates the Holliday junction
CC migration by localized denaturation and reannealing.
CC {ECO:0000255|HAMAP-Rule:MF_00016}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00016};
CC -!- SUBUNIT: Forms a complex with RuvA. {ECO:0000255|HAMAP-Rule:MF_00016}.
CC -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000255|HAMAP-
CC Rule:MF_00016}.
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DR EMBL; D84298; BAA76366.1; -; Genomic_DNA.
DR EMBL; AE000513; AAF10176.1; -; Genomic_DNA.
DR PIR; D75498; D75498.
DR RefSeq; NP_294319.1; NC_001263.1.
DR RefSeq; WP_010887241.1; NZ_CP015081.1.
DR AlphaFoldDB; Q9X719; -.
DR SMR; Q9X719; -.
DR STRING; 243230.DR_0596; -.
DR EnsemblBacteria; AAF10176; AAF10176; DR_0596.
DR KEGG; dra:DR_0596; -.
DR PATRIC; fig|243230.17.peg.774; -.
DR eggNOG; COG2255; Bacteria.
DR HOGENOM; CLU_055599_1_0_0; -.
DR InParanoid; Q9X719; -.
DR OMA; IHRMSRP; -.
DR OrthoDB; 874197at2; -.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0009378; F:four-way junction helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00016; DNA_helic_RuvB; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041445; AAA_lid_4.
DR InterPro; IPR004605; DNA_helicase_Holl-junc_RuvB.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008824; RuvB-like_N.
DR InterPro; IPR008823; RuvB_C.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR42848; PTHR42848; 1.
DR Pfam; PF17864; AAA_lid_4; 1.
DR Pfam; PF05491; RuvB_C; 1.
DR Pfam; PF05496; RuvB_N; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00635; ruvB; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA damage; DNA recombination; DNA repair; Helicase;
KW Hydrolase; Nucleotide-binding; Reference proteome; SOS response.
FT CHAIN 1..333
FT /note="Holliday junction ATP-dependent DNA helicase RuvB"
FT /id="PRO_0000165526"
FT BINDING 50..57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT CONFLICT 87
FT /note="Missing (in Ref. 1; BAA76366)"
FT /evidence="ECO:0000305"
FT CONFLICT 162..163
FT /note="SR -> RA (in Ref. 1; BAA76366)"
FT /evidence="ECO:0000305"
FT CONFLICT 214..235
FT /note="RLLRRVRDYADVAGETTIGLER -> ACCGACATTPTWRAKPPSAWN (in
FT Ref. 1; BAA76366)"
FT /evidence="ECO:0000305"
FT CONFLICT 251..266
FT /note="DDRDKKYLETLIHRFA -> GTTRQEVPRNPDSPLC (in Ref. 1;
FT BAA76366)"
FT /evidence="ECO:0000305"
FT CONFLICT 303..333
FT /note="TPRGRVATAHAYDHLGLPPGGIDDGNGIFLN -> STWPRGDGTRL (in
FT Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 333 AA; 36325 MW; 112B08F116EAB5FA CRC64;
MTAPENLDAA LRPKTLTEYV GQEKLKDKLG VYLQAARGRR EALDHTLLFG PPGLGKTTLA
HIIAYELGVN IRVTSGPAIE KPGDLAAILT NSLEEGDVLF IDEIHRLGRV AEEHLYPAME
DFKLDIVLGQ GPAARTIELP LPRFTLVGAT TRPGLITAPM RSRFGIIEHL EYYTAEEIAT
NLLRDARLLG FGLDEEAGLE IGARSRGTMR IAKRLLRRVR DYADVAGETT IGLERAQSAL
DKLGLDSAGL DDRDKKYLET LIHRFAGGPV GVDTLATAIS EDALTLEDVY EPYLIQLGFI
KRTPRGRVAT AHAYDHLGLP PGGIDDGNGI FLN
